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Type 1 diacylglycerol acyltransferases of Brassica napus preferentially incorporate oleic acid into triacylglycerol.

Aznar-Moreno J, Denolf P, Van Audenhove K, De Bodt S, Engelen S, Fahy D, Wallis JG, Browse J - J. Exp. Bot. (2015)

Bottom Line: Thorough understanding of the enzymology of oil accumulation is critical to the goal of modifying oilseeds for improved vegetable oil production.This strong sensitivity of the BnDGAT1 isozymes to the relative concentrations of acyl-CoA substrates substantially explains the observed fatty acid composition of B. napus seed oil.Understanding these enzymes that are critical for triacylglycerol synthesis will facilitate genetic and biotechnological manipulations to improve this oilseed crop.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USA.

No MeSH data available.


Related in: MedlinePlus

Sequence alignment of deduced amino acid sequences of four B. napus DGAT1 candidates (BnDGAT1-1 to BnDGAT1-4) and DGAT1 proteins from Arabidopsis thaliana (At), Ricinus communis (Rc), Olea europaea (Oe) and Theobroma cacao (Tc). Nine predicted transmembrane domains are underlined. Boxed regions are (1) acyl-CoA binding or active site, (2) thiolase acyl-enzyme binding signature, (3) DAG binding site and (4) ER retention/retrieval. Black and grey backgrounds indicate 100% and 75% conservation, respectively, among the eight sequences shown. Asterisks indicate residues conserved more widely among DGAT1 proteins (refer to text for details).
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Figure 2: Sequence alignment of deduced amino acid sequences of four B. napus DGAT1 candidates (BnDGAT1-1 to BnDGAT1-4) and DGAT1 proteins from Arabidopsis thaliana (At), Ricinus communis (Rc), Olea europaea (Oe) and Theobroma cacao (Tc). Nine predicted transmembrane domains are underlined. Boxed regions are (1) acyl-CoA binding or active site, (2) thiolase acyl-enzyme binding signature, (3) DAG binding site and (4) ER retention/retrieval. Black and grey backgrounds indicate 100% and 75% conservation, respectively, among the eight sequences shown. Asterisks indicate residues conserved more widely among DGAT1 proteins (refer to text for details).

Mentions: Within the BnDGAT family, BnDGAT1-1 and BnDGAT1-2 are 98% identical to each other in primary amino acid sequence, and BnDGAT1-3 and 1-4 likewise 97% identical. However, amino acid comparisons between these two groups show lower, ~88%, identity. Alignment of the deduced amino acid sequences of these enzymes with Arabidopsis and other plant DGAT1 sequences (Fig. 2) revealed a strong homology, which does not, however, include the first 90 amino acid residues; these first residues are known to be variable within the DGAT1 family (Turchetto-Zolet et al., 2011). The DGAT1 variable N-terminal region has been shown to allow the proteins to form homo-tetramers (McFie et al., 2010). The candidate DGAT1 proteins are predicted to include the nine putative transmembrane domains and a C-terminal ER retrieval motif characteristic of DGAT1 enzymes (Fig. 2; Turchetto-Zolet et al., 2011). Each of the proteins shares functional motifs present in the DGAT1 family, including an acyl-CoA binding and active site (Fig. 2, box 1), a DAG-binding site (Fig. 2, box 3), and a putative thiolase acyl-enzyme binding signature which includes a leucine zipper motif (Fig. 2, box 2; Cao, 2011).


Type 1 diacylglycerol acyltransferases of Brassica napus preferentially incorporate oleic acid into triacylglycerol.

Aznar-Moreno J, Denolf P, Van Audenhove K, De Bodt S, Engelen S, Fahy D, Wallis JG, Browse J - J. Exp. Bot. (2015)

Sequence alignment of deduced amino acid sequences of four B. napus DGAT1 candidates (BnDGAT1-1 to BnDGAT1-4) and DGAT1 proteins from Arabidopsis thaliana (At), Ricinus communis (Rc), Olea europaea (Oe) and Theobroma cacao (Tc). Nine predicted transmembrane domains are underlined. Boxed regions are (1) acyl-CoA binding or active site, (2) thiolase acyl-enzyme binding signature, (3) DAG binding site and (4) ER retention/retrieval. Black and grey backgrounds indicate 100% and 75% conservation, respectively, among the eight sequences shown. Asterisks indicate residues conserved more widely among DGAT1 proteins (refer to text for details).
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC4588894&req=5

Figure 2: Sequence alignment of deduced amino acid sequences of four B. napus DGAT1 candidates (BnDGAT1-1 to BnDGAT1-4) and DGAT1 proteins from Arabidopsis thaliana (At), Ricinus communis (Rc), Olea europaea (Oe) and Theobroma cacao (Tc). Nine predicted transmembrane domains are underlined. Boxed regions are (1) acyl-CoA binding or active site, (2) thiolase acyl-enzyme binding signature, (3) DAG binding site and (4) ER retention/retrieval. Black and grey backgrounds indicate 100% and 75% conservation, respectively, among the eight sequences shown. Asterisks indicate residues conserved more widely among DGAT1 proteins (refer to text for details).
Mentions: Within the BnDGAT family, BnDGAT1-1 and BnDGAT1-2 are 98% identical to each other in primary amino acid sequence, and BnDGAT1-3 and 1-4 likewise 97% identical. However, amino acid comparisons between these two groups show lower, ~88%, identity. Alignment of the deduced amino acid sequences of these enzymes with Arabidopsis and other plant DGAT1 sequences (Fig. 2) revealed a strong homology, which does not, however, include the first 90 amino acid residues; these first residues are known to be variable within the DGAT1 family (Turchetto-Zolet et al., 2011). The DGAT1 variable N-terminal region has been shown to allow the proteins to form homo-tetramers (McFie et al., 2010). The candidate DGAT1 proteins are predicted to include the nine putative transmembrane domains and a C-terminal ER retrieval motif characteristic of DGAT1 enzymes (Fig. 2; Turchetto-Zolet et al., 2011). Each of the proteins shares functional motifs present in the DGAT1 family, including an acyl-CoA binding and active site (Fig. 2, box 1), a DAG-binding site (Fig. 2, box 3), and a putative thiolase acyl-enzyme binding signature which includes a leucine zipper motif (Fig. 2, box 2; Cao, 2011).

Bottom Line: Thorough understanding of the enzymology of oil accumulation is critical to the goal of modifying oilseeds for improved vegetable oil production.This strong sensitivity of the BnDGAT1 isozymes to the relative concentrations of acyl-CoA substrates substantially explains the observed fatty acid composition of B. napus seed oil.Understanding these enzymes that are critical for triacylglycerol synthesis will facilitate genetic and biotechnological manipulations to improve this oilseed crop.

View Article: PubMed Central - PubMed

Affiliation: Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USA.

No MeSH data available.


Related in: MedlinePlus